Literature summary for 4.1.1.8 extracted from

Berthold, C.L.; Sidhu, H.; Ricagno, S.; Richards, N.G.; Lindqvist, Y.
Detection and characterization of merohedral twinning in crystals of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes (2006), Biochim. Biophys. Acta, 1764, 122-128.

Crystallization (Commentary)

Crystallization (Comment)	Organism
recombinant, hanging drop vapour-diffusion method, native and seleno-methionine labelled enzyme is crystallized in two different conditions resulting in two different crystal forms, one showing poor diffraction and the other merohedral twinning. Crystals in the former category belong to the tetragonal space group P4(2)2(1)2, crystals in the latter category are obtained by cocrystallization of the protein with coenzyme A, thiamine diphosphate and Mg2+. The crystal is heavily twinned with a twin ratio of 0.43	Oxalobacter formigenes

Crystallization (Comment)

Organism

recombinant, hanging drop vapour-diffusion method, native and seleno-methionine labelled enzyme is crystallized in two different conditions resulting in two different crystal forms, one showing poor diffraction and the other merohedral twinning. Crystals in the former category belong to the tetragonal space group P4(2)2(1)2, crystals in the latter category are obtained by cocrystallization of the protein with coenzyme A, thiamine diphosphate and Mg2+. The crystal is heavily twinned with a twin ratio of 0.43

Oxalobacter formigenes

Organism

Organism	UniProt	Comment	Textmining
Oxalobacter formigenes	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant	Oxalobacter formigenes

Synonyms

Synonyms	Comment	Organism
OXC	-	Oxalobacter formigenes

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Oxalobacter formigenes

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Release 2023.1 (January 2023)